Characterization of Membrane-bound Spermidine Dehydrogenase of<i>Citrobacter freundii</i>

Hisano, Tomohiro; Murata, Kousaku; Kimura, Akira; Matsushita, Kazunobu; Toyama, Hirohide; Adachi, Osao

doi:10.1271/bbb.56.1916

Cited by 15 publications

(9 citation statements)

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“…The SpdH of S. marcescens is a flavoprotein and that of C. freundii is a quinoprotein (Hisano et al, 1992a;Tabor & Kellogg, 1970). The P. aeruginosa SpdH does not appear to be a quinoprotein, because it has no sequence similarity to known quinoproteins that have a conserved pyrroloquinoline quinone (PQQ)-binding domain and a homologous haem C-binding sequence in the carboxyl-terminal region (Oubrie, 2003;Yamada et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

“…However, the impaired growth of spuA and spuB mutants on spermidine and spermine suggests that the SpuA and SpuB enzymes play major roles in the catabolism of these polyamines. In addition, P. aeruginosa expresses spermidine dehydrogenase (SpdH; EC 1.5.99.6), which has also been identified in Citrobacter freundii and Serratia marcesens (Hisano et al, 1990(Hisano et al, , 1992aTabor & Kellogg, 1970). The SpdH of P. aeruginosa IFO3080 is constitutively expressed and has been purified as a 63 kDa monomer, but it remains to be characterized in detail (Hisano et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

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Characterization and a role of Pseudomonas aeruginosa spermidine dehydrogenase in polyamine catabolism

et al. 2006

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Pseudomonas aeruginosa PAO1 has two possible catabolic pathways of spermidine and spermine; one includes the spuA and spuB products with unknown functions and the other involves spermidine dehydrogenase (SpdH; EC 1.5.99.6) encoded by an unknown gene. The properties of SpdH in P. aeruginosa PAO1 were characterized and the corresponding spdH gene in this strain identified. The deduced SpdH (620 residues, calculated M r of 68 861) had a signal sequence of 28 amino acids at the amino terminal and a potential transmembrane segment between residues 76 and 92, in accordance with membrane location of the enzyme. Purified SpdH oxidatively cleaved spermidine into 1,3-diaminopropane and 4-aminobutyraldehyde with a specific activity of 37 units (mg protein) "1 and a K m value of 36 mM. The enzyme also hydrolysed spermine into spermidine and 3-aminopropanaldehyde with a specific activity of 25 units (mg protein) "1 and a K m of 18 mM. Knockout of spdH had no apparent effect on the utilization of both polyamines, suggesting that this gene is minimally involved in polyamine catabolism. However, when spdH was fused to the polyamine-inducible promoter of spuA, it fully restored the ability of a spuA mutant to utilize spermidine. It is concluded that SpdH can perform a catabolic role in vivo, but P. aeruginosa PAO1 does not produce sufficient amounts of the enzyme to execute this function.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization and a role of Pseudomonas aeruginosa spermidine dehydrogenase in polyamine catabolism

et al. 2006

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“…The accumulation of diaminopropane can only be explained by catabolism of spermidine. Spermidine dehydrogenase activities have been reported in the γ‐proteobacteria Citrobacter freudii , Serratia marcescens and P. aeruginosa (Tabor and Kellogg, 1970; Hisano et al ., 1992; Dasu et al ., 2006). Each of these spermidine dehydrogenases cleaves spermidine to release diaminopropane and 4‐aminobutyraldehyde.…”

Section: Discussionmentioning

confidence: 99%

Independent evolutionary origins of functional polyamine biosynthetic enzyme fusions catalysingde novodiamine to triamine formation

Green

Hanfrey

Elliott

et al. 2011

Molecular Microbiology

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Summary We have identified gene fusions of polyamine biosynthetic enzymes S-adenosylmethionine decarboxylase (AdoMetDC, speD) and aminopropyltransferase (speE) orthologues in diverse bacterial phyla. Both domains are functionally active and we demonstrate the novel de novo synthesis of the triamine spermidine from the diamine putrescine by fusion enzymes from β-proteobacterium Delftia acidovorans and δ-proteobacterium Syntrophus aciditrophicus, in a ΔspeDE gene deletion strain of Salmonella enterica sv. Typhimurium. Fusion proteins from marine α-proteobacterium Candidatus Pelagibacter ubique, actinobacterium Nocardia farcinica, chlorobi species Chloroherpeton thalassium, and β-proteobacterium Delftia acidovorans each produce a different profile of non-native polyamines including sym-norspermidine when expressed in Escherichia coli. The different aminopropyltransferase activities together with phylogenetic analysis confirm independent evolutionary origins for some fusions. Comparative genomic analysis strongly indicates that gene fusions arose by merger of adjacent open reading frames. Independent fusion events, and horizontal and vertical gene transfer contributed to the scattered phyletic distribution of the gene fusions. Surprisingly, expression of fusion genes in E. coli and S. Typhimurium revealed novel latent spermidine catabolic activity producing non-native 1,3-diaminopropane in these species. We have also identified fusions of polyamine biosynthetic enzymes agmatine deiminase and N-carbamoylputrescine amidohydrolase in archaea, and of S-adenosylmethionine decarboxylase and ornithine decarboxylase in the single-celled green alga Micromonas.

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“…In some bacterial species, such as Pseudomonas aeruginosa, Citrobacter freundii and Serratia marcesens, Spd is oxidized by spermidine dehydrogenases with FAD and/or heme as prosthetic groups [38][39][40] . Reaction products of these enzymes with Spd are Dap and 4-aminobutanal, indicating cleavage at the endo-side of the N 4 -nitrogen.…”

mentioning

confidence: 99%

“…Reaction products of these enzymes with Spd are Dap and 4-aminobutanal, indicating cleavage at the endo-side of the N 4 -nitrogen. The P. aerugonosa enzyme (SpdH) oxidizes also Spm through an exo-mode producing Spd and 3-aminopropanal [38][39][40][41] . In several bacterial species, an FAD-dependent amine oxidase classified as putrescine oxidase (PuO) is also present.…”

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confidence: 99%

The tree of life of polyamine oxidases

Salvi

Tavladoraki

2020

Sci Rep

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Polyamine oxidases (PAOs) are characterized by a broad variability in catalytic properties and subcellular localization, and impact key cellular processes in diverse organisms. In the present study, a comprehensive phylogenetic analysis was performed to understand the evolution of PAOs across the three domains of life and particularly within eukaryotes. Phylogenetic trees show that PAO-like sequences of bacteria, archaea, and eukaryotes form three distinct clades, with the exception of a few procaryotes that probably acquired a PAO gene through horizontal transfer from a eukaryotic donor. Results strongly support a common origin for archaeal PAO-like proteins and eukaryotic PAOs, as well as a shared origin between PAOs and monoamine oxidases. Within eukaryotes, four main lineages were identified that likely originated from an ancestral eukaryotic PAO before the split of the main superphyla, followed by specific gene losses in each superphylum. Plant PAOs show the highest diversity within eukaryotes and belong to three distinct clades that underwent to multiple events of gene duplication and gene loss. Peptide deletion along the evolution of plant PAOs of Clade I accounted for further diversification of function and subcellular localization. This study provides a reference for future structure–function studies and emphasizes the importance of extending comparisons among PAO subfamilies across multiple eukaryotic superphyla.

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Characterization of Membrane-bound Spermidine Dehydrogenase ofCitrobacter freundii

Cited by 15 publications

References 3 publications

Characterization and a role of Pseudomonas aeruginosa spermidine dehydrogenase in polyamine catabolism

Characterization and a role of Pseudomonas aeruginosa spermidine dehydrogenase in polyamine catabolism

Independent evolutionary origins of functional polyamine biosynthetic enzyme fusions catalysingde novodiamine to triamine formation

The tree of life of polyamine oxidases

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